Selective oxidative modification of tryptophan and cysteine residues using visible light responsive Rh doped SrTiO3 photocatalyst

S Sho Usuki (Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-0012, Japan) N Naoko Taki (Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-0012, Japan) Y Yuma Uesaka (Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-0012, Japan) H Haru Togawa (Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-0012, Japan) S Shanhu Liu (Henan Joint International Research Laboratory of Environmental Pollution Control Materials, Henan Key Laboratory of Polyoxometalate Chemistry, College of Chemistry and Chemical Engineering) K Kenji Yamatoya K Kazuya Nakata (Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-0012, Japan)

Abstract

Abstract In recent years, amino acids and peptides have attracted significant attention in food and medical fields due to their functionality. These functionalities largely depend on the chemical properties of their side chains, and efficient methods for selective side chain modification are desired. In this study, we investigated the selective modification of amino acids and peptides using rhodium-doped SrTiO3 (g-STO:Rh), a visible light-responsive photocatalyst. HPLC and LCMS analyses revealed that g-STO:Rh exhibited selective reactivity toward tryptophan and cysteine among the 20 protein-constituent amino acids. While cysteine was oxidatively dimerized to cystine, tryptophan underwent selective oxidation of its indole ring side chain, forming N-formylkynurenine. Furthermore, studies on dipeptides and tripeptides containing tryptophan have demonstrated that selective oxidation proceeds similarly to tryptophan residues within peptides.

Article Details

Volume / Issue Vol. 15, Issue 1
Published July 01, 2025
ISSN 2045-2322
Publisher Nature Portfolio

Journal Info

Scientific Reports

Nature Portfolio

ISSN: 2045-2322 Open Access Life Sciences

Authors (7)

S

Sho Usuki

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-0012, Japan

N

Naoko Taki

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-0012, Japan

Y

Yuma Uesaka

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-0012, Japan

H

Haru Togawa

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-0012, Japan

S

Shanhu Liu

Henan Joint International Research Laboratory of Environmental Pollution Control Materials, Henan Key Laboratory of Polyoxometalate Chemistry, College of Chemistry and Chemical Engineering

K

Kenji Yamatoya

K

Kazuya Nakata

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-0012, Japan